메뉴 건너뛰기




Volumn 66, Issue 2, 2004, Pages 228-239

High-affinity interactions between human α1A-adrenoceptor C-terminal splice variants produce homo- and heterodimers but do not generate the α1L-adrenoceptor

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1A ADRENERGIC RECEPTOR; ALPHA 1L ADRENERGIC RECEPTOR; ALPHA ADRENERGIC RECEPTOR; DELTA OPIATE RECEPTOR; DIMER; G PROTEIN COUPLED RECEPTOR; GREEN FLUORESCENT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); HYBRID PROTEIN; LUCIFERASE; OLIGOMER; PRAZOSIN; RADIOLIGAND; SULFUR 35; UNCLASSIFIED DRUG;

EID: 3342934656     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.66.2.228     Document Type: Article
Times cited : (57)

References (44)
  • 2
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub MA, Couturier C, Lucas-Meunier E, Angers S, Fossier P, Bouvier M, and Jockers R (2002) Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J Biol Chem 277:21522-21528.
    • (2002) J Biol Chem , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1    Couturier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5    Bouvier, M.6    Jockers, R.7
  • 3
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • Baneres JL and Parello J (2003) Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J Mol Biol 329:815-829.
    • (2003) J Mol Biol , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 4
    • 0037862083 scopus 로고    scopus 로고
    • The 'magic tail' of G protein-coupled receptors: An anchorage for functional protein networks
    • Bockaert J, Marin P, Dumuis A, and Fagni L (2003) The 'magic tail' of G protein-coupled receptors: an anchorage for functional protein networks. FEBS Lett 546: 65-72.
    • (2003) FEBS Lett , vol.546 , pp. 65-72
    • Bockaert, J.1    Marin, P.2    Dumuis, A.3    Fagni, L.4
  • 6
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier M (2001) Oligomerization of G-protein-coupled transmitter receptors. Nat Rev Neurosci 2:274-288.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 274-288
    • Bouvier, M.1
  • 7
    • 0032562288 scopus 로고    scopus 로고
    • Agonist occupation of an α2A-adrenoreceptor-Gilα fusion protein results in activation of both receptor-linked and endogenous Gi proteins. Comparisons of their contributions to GTPase activity and signal transduction and analysis of receptor-G protein activation stoichiometry
    • Burt AR, Sautel M, Wilson MA, Rees S, Wise A, and Milligan G (1998) Agonist occupation of an α2A-adrenoreceptor-Gilα fusion protein results in activation of both receptor-linked and endogenous Gi proteins. Comparisons of their contributions to GTPase activity and signal transduction and analysis of receptor-G protein activation stoichiometry. J Biol Chem 273:10367-10375.
    • (1998) J Biol Chem , vol.273 , pp. 10367-10375
    • Burt, A.R.1    Sautel, M.2    Wilson, M.A.3    Rees, S.4    Wise, A.5    Milligan, G.6
  • 8
    • 0142149074 scopus 로고    scopus 로고
    • Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins
    • Carrillo JJ, Pediani J, and Milligan G (2003) Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins. J Biol Chem 278:42578-42587.
    • (2003) J Biol Chem , vol.278 , pp. 42578-42587
    • Carrillo, J.J.1    Pediani, J.2    Milligan, G.3
  • 11
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the δ opioid receptor: Implication for a role in receptor internalization
    • Cvejic S and Devi LA (1997) Dimerization of the δ opioid receptor: implication for a role in receptor internalization. J Biol Chem 273: 26959-26964.
    • (1997) J Biol Chem , vol.273 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 12
    • 0032442115 scopus 로고    scopus 로고
    • Cellular localization and pharmacological characterization of functioning alpha-1 adrenoceptors by fluorescent ligand binding and image analysis reveals identical binding properties of clustered and diffuse populations of receptors
    • Daly CJ, Milligan CM, Milligan G, Mackenzie JF, and McGrath JC (1998) Cellular localization and pharmacological characterization of functioning alpha-1 adrenoceptors by fluorescent ligand binding and image analysis reveals identical binding properties of clustered and diffuse populations of receptors J Pharmacol Exp Ther 286:984-990.
    • (1998) J Pharmacol Exp Ther , vol.286 , pp. 984-990
    • Daly, C.J.1    Milligan, C.M.2    Milligan, G.3    Mackenzie, J.F.4    McGrath, J.C.5
  • 13
    • 0035478438 scopus 로고    scopus 로고
    • Heterodimerization of G protein-coupled receptors: Pharmacology, signaling and trafficking
    • Devi LA (2001) Heterodimerization of G protein-coupled receptors: pharmacology, signaling and trafficking. Trends Pharmacol Sci 22:532-537.
    • (2001) Trends Pharmacol Sci , vol.22 , pp. 532-537
    • Devi, L.A.1
  • 14
    • 0032555657 scopus 로고    scopus 로고
    • Agonist-induced internalization of the G protein G11α and thyrotropin-releasing hormone receptors proceed on different time scales
    • Drmota T, Novotny J, Kim GD, Eidne KA, Milligan G, and Svoboda P (1998) Agonist-induced internalization of the G protein G11α and thyrotropin-releasing hormone receptors proceed on different time scales. J Biol Chem 273:21699-21707.
    • (1998) J Biol Chem , vol.273 , pp. 21699-21707
    • Drmota, T.1    Novotny, J.2    Kim, G.D.3    Eidne, K.A.4    Milligan, G.5    Svoboda, P.6
  • 15
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • Eidne KA, Kroeger KM, and Hanyaloglu AC (2002) Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells. Trends Endocrinol Metabol 13:415-421.
    • (2002) Trends Endocrinol Metabol , vol.13 , pp. 415-421
    • Eidne, K.A.1    Kroeger, K.M.2    Hanyaloglu, A.C.3
  • 16
    • 0030790446 scopus 로고    scopus 로고
    • Pharmacological pleiotropism of the human recombinant alpha1A-adrenoceptor: Implications for alpha1-adrenoceptor classification
    • Ford AP, Daniels DV, Chang DJ, Gever JR, Jasper JR, Lesnick JD, and Clarke DE (1997) Pharmacological pleiotropism of the human recombinant alpha1A-adrenoceptor: implications for alpha1-adrenoceptor classification. Br J Pharmacol 121:1127-1135.
    • (1997) Br J Pharmacol , vol.121 , pp. 1127-1135
    • Ford, A.P.1    Daniels, D.V.2    Chang, D.J.3    Gever, J.R.4    Jasper, J.R.5    Lesnick, J.D.6    Clarke, D.E.7
  • 17
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups and fingerprints
    • Fredriksson R, Lagerstrom MC, Lundin LG, and Schioth HB (2003) The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups and fingerprints. Mol Pharmacol 63:1256-1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 19
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George SR, O'Dowd BF, and Lee SP (2002) G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat Rev Drug Discov 1:808-820.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 20
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine d2 receptor homodimer
    • Guo W, Shi L, and Javitch JA (2003) The fourth transmembrane segment forms the interface of the dopamine d2 receptor homodimer. J Biol Chem 278:4385-4388.
    • (2003) J Biol Chem , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 22
    • 0030864213 scopus 로고    scopus 로고
    • Subtype-specific differences in subcellular localization of α1-adrenoceptors: Chlorethylclonidine preferentially alkylates the accessible cell surface alpha1-adrenoceptors irrespective of the subtype
    • Hirasawa A, Sugawara T, Awaji T, Tsumaya K, Ito H, and Tsujimoto G (1997) Subtype-specific differences in subcellular localization of α1-adrenoceptors: chlorethylclonidine preferentially alkylates the accessible cell surface alpha1-adrenoceptors irrespective of the subtype Mol Pharmacol 52:764-770.
    • (1997) Mol Pharmacol , vol.52 , pp. 764-770
    • Hirasawa, A.1    Sugawara, T.2    Awaji, T.3    Tsumaya, K.4    Ito, H.5    Tsujimoto, G.6
  • 23
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • Jordan BA and Devi LA (1999) G-protein-coupled receptor heterodimerization modulates receptor function. Nature (Lond) 399:697-700.
    • (1999) Nature (Lond) , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 24
    • 0346996861 scopus 로고    scopus 로고
    • Functional interactions between μ opioid and α2A-adrenergic receptors
    • Jordan BA, Gomes I, Rios C, Filipovska J, and Devi LA (2003) Functional interactions between μ opioid and α2A-adrenergic receptors. Mol Pharmacol 64:1317-1324.
    • (2003) Mol Pharmacol , vol.64 , pp. 1317-1324
    • Jordan, B.A.1    Gomes, I.2    Rios, C.3    Filipovska, J.4    Devi, L.A.5
  • 25
    • 0035793079 scopus 로고    scopus 로고
    • Oligomerization of opioid receptors with β2-adrenergic receptors: A role in trafficking and mitogen-activated protein kinase activation
    • Jordan BA, Trapaidze N, Gomes I, Nivarthi R, and Devi LA (2001) Oligomerization of opioid receptors with β2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation. Proc Natl Acad Sci USA 98:343-348.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 343-348
    • Jordan, B.A.1    Trapaidze, N.2    Gomes, I.3    Nivarthi, R.4    Devi, L.A.5
  • 26
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y, Fotiadis D, Filipek S, Saperstein DA, Palczewski K, and Engel A (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J Biol Chem 278: 21655-21662.
    • (2003) J Biol Chem , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 27
    • 0037067773 scopus 로고    scopus 로고
    • Effective information transfer from the α1b-adrenoceptor to Gα 11 requires both β/γ interactions and an aromatic group four amino acids from the C terminus of the G protein
    • Liu S, Carrillo JJ, Pediani J, and Milligan G (2002) Effective information transfer from the α1b-adrenoceptor to Gα 11 requires both β/γ interactions and an aromatic group four amino acids from the C terminus of the G protein J Biol Chem 277:25707-25714.
    • (2002) J Biol Chem , vol.277 , pp. 25707-25714
    • Liu, S.1    Carrillo, J.J.2    Pediani, J.3    Milligan, G.4
  • 28
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer: The human δ opioid receptor displays constitutive oligomerization at the cell surface which is not regulated by receptor occupancy
    • McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, and Milligan G (2001) Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer: the human δ opioid receptor displays constitutive oligomerization at the cell surface which is not regulated by receptor occupancy. J Biol Chem 276:14092-14099.
    • (2001) J Biol Chem , vol.276 , pp. 14092-14099
    • McVey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 30
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier JF, Salahpour A, Angers S, Breit A, and Bouvier M (2002) Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 277:44925-44931.
    • (2002) J Biol Chem , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 31
    • 0035032316 scopus 로고    scopus 로고
    • Oligomerisation of G-protein-coupled receptors
    • Milligan G (2001) Oligomerisation of G-protein-coupled receptors. J Cell Sci 114: 1265-1271.
    • (2001) J Cell Sci , vol.114 , pp. 1265-1271
    • Milligan, G.1
  • 32
    • 0037305047 scopus 로고    scopus 로고
    • 35S]GTP gamma S binding assays
    • 35S]GTP gamma S binding assays. Trends Pharmacol Sci 24:87-90.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 87-90
    • Milligan, G.1
  • 33
    • 0035478746 scopus 로고    scopus 로고
    • Protein-protein interactions at G-protein-coupled receptors
    • Milligan G and White JH (2001) Protein-protein interactions at G-protein-coupled receptors. Trends Pharmacol Sci 22:513-518.
    • (2001) Trends Pharmacol Sci , vol.22 , pp. 513-518
    • Milligan, G.1    White, J.H.2
  • 34
    • 0027244086 scopus 로고
    • Enhanced degradation of the phosphoinositidase C-linked guanine-nucleotide-binding protein Gq alpha/G11 alpha following activation of the human M1 muscarinic acetylcholine receptor expressed in CHO cells
    • Mitchell FM, Buckley NJ, and Milligan G (1993) Enhanced degradation of the phosphoinositidase C-linked guanine-nucleotide-binding protein Gq alpha/G11 alpha following activation of the human M1 muscarinic acetylcholine receptor expressed in CHO cells. Biochem J 293:495-499.
    • (1993) Biochem J , vol.293 , pp. 495-499
    • Mitchell, F.M.1    Buckley, N.J.2    Milligan, G.3
  • 35
    • 0038521270 scopus 로고    scopus 로고
    • Promiscuous coupling at receptor-Gα fusion proteins. The receptor of one covalent complex interacts with the α-subunit of another
    • Molinari P, Ambrosio C, Riitano D, Sbraccia M, Gro C, and Costa T (2003) Promiscuous coupling at receptor-Gα fusion proteins. The receptor of one covalent complex interacts with the α-subunit of another. J Biol Chem 278:15778-15788.
    • (2003) J Biol Chem , vol.278 , pp. 15778-15788
    • Molinari, P.1    Ambrosio, C.2    Riitano, D.3    Sbraccia, M.4    Gro, C.5    Costa, T.6
  • 36
    • 0036829815 scopus 로고    scopus 로고
    • The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor
    • Overton MC and Blumer KJ (2002) The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor. J Biol Chem 277:41463-41472.
    • (2002) J Biol Chem , vol.277 , pp. 41463-41472
    • Overton, M.C.1    Blumer, K.J.2
  • 37
    • 0034742707 scopus 로고    scopus 로고
    • αl-Adrenergic receptors: New insights and directions
    • Piascik MT and Perez DM (2001) αl-Adrenergic receptors: new insights and directions. J Pharmacol Exp Ther 298:403-410.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 403-410
    • Piascik, M.T.1    Perez, D.M.2
  • 38
    • 0035545309 scopus 로고    scopus 로고
    • Clinical significance of alpha1-adrenoceptor selectivity in the management of benign prostatic hyperplasia
    • Pool JL and Kirby RS (2001) Clinical significance of alpha1-adrenoceptor selectivity in the management of benign prostatic hyperplasia. Int Urol Nephrol 33:407-412.
    • (2001) Int Urol Nephrol , vol.33 , pp. 407-412
    • Pool, J.L.1    Kirby, R.S.2
  • 39
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and heterooligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • Ramsay D, Kellett E, McVey M, Rees S, and Milligan G (2002) Homo- and heterooligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences. Biochem J 365:429-440.
    • (2002) Biochem J , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 40
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • Rocheville M, Lange DC, Kumar U, Patel SC, Patel RC, and Patel YC (2000) Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity. Science (Wash DC) 288:154-157.
    • (2000) Science (Wash DC) , vol.288 , pp. 154-157
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Patel, S.C.4    Patel, R.C.5    Patel, Y.C.6
  • 43
    • 0346366929 scopus 로고    scopus 로고
    • Subtype-specific dimerization of α1-adrenoceptors: Effects on receptor expression and pharmacological properties
    • Uberti MA, Hall RA, and Minneman KP (2003) Subtype-specific dimerization of α1-adrenoceptors: effects on receptor expression and pharmacological properties. Mol Pharmacol 64:1379-1390.
    • (2003) Mol Pharmacol , vol.64 , pp. 1379-1390
    • Uberti, M.A.1    Hall, R.A.2    Minneman, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.